eF-site ID 1r9x-A PDB Code 1r9x Chain A click to enlarge Title Bacterial cytosine deaminase D314G mutant. Classification HYDROLASE Compound Cytosine deaminase Source Escherichia coli (strain K12) (CODA_ECOLI) Sequence A:  ALQTIINARLPGEEGLWQIHLQDGKISAIDAQSGVMPITE NSLDAEQGLVIPPFVEPHIHLDTTQTAGQPNWNQSGTLFE GIERWAERKALLTHDDVKQRAWQTLKWQIANGIQHVRTHV DVSDATLTALKAMLEVKQEVAPWIDLQIVAFPQEGILSYP NGEALLEEALRLGADVVGAIPHFEFTREYGVESLHKTFAL AQKYDRLIDVHCDEIDDEQSRFVETVAALAHHEGMGARVT ASHTTAMHSYNGAYTSRLFRLLKMSGINFVANPLVNIHLQ GRFDTYPKRRGITRVKEMLESGINVCFGHDGVFDPWYPLG TANMLQVLHMGLHVCQLMGYGQINDGLNLITHHSARTLNL QDYGIAAGNSANLIILPAENGFDALRRQVPVRYSVRGGKV IASTQPAQTTVYLEQPEAIDYKR Description Functional site 1) chain A residue 61 type sequence H description BINDING SITE FOR RESIDUE FE A 501 source : AC1 2) chain A residue 63 type sequence H description BINDING SITE FOR RESIDUE FE A 501 source : AC1 3) chain A residue 214 type sequence H description BINDING SITE FOR RESIDUE FE A 501 source : AC1 4) chain A residue 313 type sequence D description BINDING SITE FOR RESIDUE FE A 501 source : AC1 5) chain A residue 128 type sequence A description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 6) chain A residue 134 type sequence K description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 7) chain A residue 171 type sequence E description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 8) chain A residue 171 type sequence E description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 9) chain A residue 174 type sequence R description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 10) chain A residue 175 type sequence L description BINDING SITE FOR RESIDUE GOL A 503 source : AC3 11) chain A residue 61 type catalytic sequence H description 710 source MCSA : MCSA1 12) chain A residue 63 type catalytic sequence H description 710 source MCSA : MCSA1 13) chain A residue 156 type catalytic sequence Q description 710 source MCSA : MCSA1 14) chain A residue 214 type catalytic sequence H description 710 source MCSA : MCSA1 15) chain A residue 217 type catalytic sequence E description 710 source MCSA : MCSA1 16) chain A residue 313 type catalytic sequence D description 710 source MCSA : MCSA1 17) chain A residue 217 type ACT_SITE sequence E description Proton donor => ECO:0000305|PubMed:11812140, ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 246 type SITE sequence H description Activates the nucleophilic water => ECO:0000305|PubMed:21545144, ECO:0000305|PubMed:21604715 source Swiss-Prot : SWS_FT_FI5 19) chain A residue 61 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 63 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 214 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 313 type BINDING sequence D description BINDING => ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|Ref.14 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 156 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 319 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11812140, ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144 source Swiss-Prot : SWS_FT_FI4

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